Evidence map›Paper›PMID 24418317›Full record

ArticleArchives of biochemistry and biophysics2014

Ca(2+)-regulatory function of the inhibitory peptide region of cardiac troponin I is aided by the C-terminus of cardiac troponin T: Effects of familial hypertrophic cardiomyopathy mutations cTnI R145G and cTnT R278C, alone and in combination, on filament sliding.

Nicolas M Brunet, P Bryant Chase, Goran Mihajlović, Brenda Schoffstall

Abstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  3. Review
  4. Article
  5. Article
  6. Novel Mutation Lys30Glu in theInternational journal of molecular sciences · 2024
    Article
  7. Article
  8. Structural and Functional Properties of Kappa Tropomyosin.International journal of molecular sciences · 2023
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Nicolas M BrunetInstitute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA.
P Bryant ChaseInstitute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA; Department of Biological Science, Florida State University, Tallahassee, FL 32306, USA. Electronic address: chase@bio.fsu.edu.
Goran MihajlovićDepartment of Physics, Florida State University, Tallahassee, FL 32306, USA.
Brenda SchoffstallInstitute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA.

Funding

ALTERED CALCIUM REGULATION IN CARDIOMYOPATHIESR01HL063974 · NHLBI · UNIVERSITY OF WASHINGTON · PI CHASE, P. BRYANT · 2001 to 2004
$1.3M
NHLBI NIH HHS HL63974NHLBI NIH HHS R01 HL063974
6 · The paper itself

Abstract

Investigations of cardiomyopathy mutations in Ca(2+) regulatory proteins troponin and tropomyosin provide crucial information about cardiac disease mechanisms, and also provide insights into functional domains in the affected polypeptides. Hypertrophic cardiomyopathy-associated mutations TnI R145G, located within the inhibitory peptide (Ip) of human cardiac troponin I (hcTnI), and TnT R278C, located immediately C-terminal to the IT arm in human cardiac troponin T (hcTnT), share some remarkable features: structurally, biochemically, and pathologically. Using bioinformatics, we find compelling evidence that TnI and TnT, and more specifically the affected regions of hcTnI and hcTnT, may be related not just structurally but also evolutionarily. To test for functional interactions of these mutations on Ca(2+)-regulation, we generated and characterized Tn complexes containing either mutation alone, or both mutations simultaneously. The most important results from in vitro motility assays (varying [Ca(2+)], temperature or HMM density) show that the TnT mutant "rescued" some deleterious effects of the TnI mutant at high Ca(2+), but exacerbated the loss of function, i.e., switching off the actomyosin interaction, at low Ca(2+). Taken together, our experimental results suggest that the C-terminus of cTnT aids Ca(2+)-regulatory function of cTnI Ip within the troponin complex.

Indexed as

Actin CytoskeletonAmino Acid SequenceAnimalsCalciumCardiomyopathy, Hypertrophic, FamilialEvolution, MolecularHumansMaleModels, MolecularMolecular Sequence DataMyosinsPoint MutationRabbitsRecombinant ProteinsSequence AlignmentTroponin ICalciumMyosinsRecombinant ProteinsTroponin ITroponin TEvolutionMotility assayTemperatureThin filament

Identifiers

PMID24418317
PMCPMC4043889

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.